ID   A0A0G0IDB9_9BACT        Unreviewed;       389 AA.
AC   A0A0G0IDB9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:KKQ52542.1};
GN   ORFNames=US70_C0008G0029 {ECO:0000313|EMBL:KKQ52542.1};
OS   Parcubacteria group bacterium GW2011_GWD2_38_11.
OC   Bacteria.
OX   NCBI_TaxID=1618941 {ECO:0000313|EMBL:KKQ52542.1, ECO:0000313|Proteomes:UP000034843};
RN   [1] {ECO:0000313|EMBL:KKQ52542.1, ECO:0000313|Proteomes:UP000034843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKQ52542.1}.
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DR   EMBL; LBTZ01000008; KKQ52542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0IDB9; -.
DR   STRING; 1618941.US70_C0008G0029; -.
DR   PATRIC; fig|1618941.3.peg.358; -.
DR   Proteomes; UP000034843; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          314..380
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   389 AA;  42102 MW;  A8E99DD820DF1C2B CRC64;
     MSEKSVTIKN VVKISLILLV IFGVGGIGGV YFDQQVLPFI RTNKHLSRIN FLKHSAENVT
     VINKTEQVTI KEDDSINEVA SQASNAVVNI ISLGSQKDLA TRMTKNTDQS GTGIIVTSDG
     LIATYRSAII EKNATYKVLL FNGANYDAKL LGIDEFSDLA FLKIEATNLT AISFGDSSRV
     YPGKKLVAIG NSFGEYQNRY ASGLLSNLAK TYNLAGKTVS SSEKLEGVFE SDFNNQKEYV
     GGPVIGYSGD LIGINGAIVV DGQNQYFQIP SNIVQKAVGL ALSNELENRP FLGAYYVSIT
     KEYAIAHSLN RDRGALIFSP SGKQGLAVIA FSPAEKAGLK INDIVLAVND QNINLDNPLS
     NLISQYKKGD EIKLLIDREG SEVKISVKL
//